Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase.

Abstract

Class I fructose-1,6-bisphosphate aldolases catalyze the interconversion between the enamine and iminium covalent enzymatic intermediates by stereospecific exchange of the pro(S) proton of the dihydroxyacetone-phosphate C3 carbon, an obligatory reaction step during substrate cleavage. To investigate the mechanism of stereospecific proton exchange, high… (More)

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Cite this paper

@article{StJean2007StereospecificPT, title={Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase.}, author={Miguel St-Jean and Jurgen Sygusch}, journal={The Journal of biological chemistry}, year={2007}, volume={282 42}, pages={31028-37} }